Emelie Vilhelmsson Wesén

Post doc at Chemical Biology

Emelie Lindahl Wesén is since 2014 a PhD student in Elin Esbjörner Winters’ research group at the division of Chemical Biology. Her research is focused on studying the uptake and intracellular vesicular transport of amyloid-β, a peptide that aggregates and accumulates in the brain of patients suffering from Alzheimer’s disease. Cultured human cells are used as a disease model and the their interaction with amyloid-β is studied using primarily confocal microscopy and flow cytometry. The long-term goal of this research project is to understand the molecular and cellular mechanisms underlying prion-like transfer of misfolded proteins.

Source: chalmers.se
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Showing 8 publications


The Liver and Kidneys mediate clearance of cardiac troponin in the rat

Aida Muslimovic, Vincent Fridén, Olav Tenstad et al
Scientific Reports. Vol. 10 (1)
Journal article

Correlation between Cellular Uptake and Cytotoxicity of Fragmented α-Synuclein Amyloid Fibrils Suggests Intracellular Basis for Toxicity

Xiaolu Zhang, Emelie Vilhelmsson Wesén, Ranjeet Kumar et al
ACS Chemical Neuroscience. Vol. 11 (3), p. 233-241
Journal article

Role of Membrane Tension Sensitive Endocytosis and Rho GTPases in the Uptake of the Alzheimer's Disease Peptide Aβ(1-42)

Emelie Vilhelmsson Wesén, Richard Lundmark, Elin Esbjörner Winters
ACS Chemical Neuroscience. Vol. 11 (13), p. 1925-1936
Journal article

Cell surface proteoglycan-mediated uptake and accumulation of the Alzheimer's disease peptide Aβ(1–42)

Emelie Vilhelmsson Wesén, Audrey Gallud, Alexandra Paul et al
Biochimica et Biophysica Acta - Biomembranes. Vol. 1860 (11), p. 2204-2214
Journal article

Lipid membranes catalyse the fibril formation of the amyloid-? (1–42) peptide through lipid-fibril interactions that reinforce secondary pathways

David Lindberg, Emelie Vilhelmsson Wesén, Johan Björkeroth et al
Biochimica et Biophysica Acta - Biomembranes. Vol. 1859 (10), p. 1921-1929
Journal article

Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1-42) compared to Aβ(1-40)

Emelie Vilhelmsson Wesén, Gavin Jeffries, Maria Matson Dzebo et al
Scientific Reports. Vol. 7 (1)
Journal article

Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

David Lindberg, Anna Wenger, Elin Sundin et al
Biochemistry. Vol. 56 (16), p. 2170-2174
Journal article

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